DHRS7

DHRS7
Identifiers
Aliases	DHRS7 , SDR34C1, retDSR4, retSDR4, CGI-86, dehydrogenase/reductase (SDR family) member 7, dehydrogenase/reductase 7
External IDs	OMIM: 612833 MGI: 1913625 HomoloGene: 9350 GeneCards: DHRS7
Gene location (Human)
Chr.	Chromosome 14 (human)
End	60,169,856 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	72,711,683 bp
RNA expression pattern
	Top expressed in
	parotid gland; ; gastrocnemius muscle; ; Achilles tendon; ; Left adrenal gland; ; blood; ; seminal vesicula; ; monocyte; ; body of stomach; ; minor salivary gland; ; prostate;
	Top expressed in
	lacrimal gland; ; parotid gland; ; brown adipose tissue; ; lip; ; adrenal gland; ; seminal vesicula; ; mammary gland; ; white adipose tissue; ; interventricular septum; ; submandibular gland;
	More reference expression data
	n/a
Orthologs
	51635
	66375
	ENSG00000100612
	ENSMUSG00000021094
	Q9Y394
	Q9CXR1
	NM_016029 ; NM_001322280 ; NM_001322281 ; NM_001322282
	NM_025522
	NP_001309209 ; NP_001309210 ; NP_001309211 ; NP_057113
	NP_079798
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated January 30, 2023

Dehydrogenase/reductase (SDR family) member 7 is a protein that in humans is encoded by the DHRS7 gene.^[5]

Function

Short-chain dehydrogenases/reductases (SDRs), such as DHRS7, catalyze the oxidation/reduction of a wide range of substrates, including retinoids and steroids.^[6]^[7]

Related Research Articles

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11β-Hydroxysteroid dehydrogenase type 1, also known as cortisone reductase, is an NADPH-dependent enzyme highly expressed in key metabolic tissues including liver, adipose tissue, and the central nervous system. In these tissues, HSD11B1 reduces cortisone to the active hormone cortisol that activates glucocorticoid receptors. It belongs to the family of short-chain dehydrogenases. It is encoded by the HSD11B1 gene.

17β-Hydroxysteroid dehydrogenases, also 17-ketosteroid reductases (17-KSR), are a group of alcohol oxidoreductases which catalyze the reduction of 17-ketosteroids and the dehydrogenation of 17β-hydroxysteroids in steroidogenesis and steroid metabolism. This includes interconversion of DHEA and androstenediol, androstenedione and testosterone, and estrone and estradiol.

17β-Hydroxysteroid dehydrogenase 1 (17β-HSD1) is an enzyme that in humans is encoded by the HSD17B1 gene. This enzyme oxidizes or reduces the C17 hydroxy/keto group of androgens and estrogens and hence is able to regulate the potency of these sex steroids

17-β-Hydroxysteroid dehydrogenase X (HSD10) also known as 3-hydroxyacyl-CoA dehydrogenase type-2 is a mitochondrial enzyme that in humans is encoded by the HSD17B10 gene. Several alternatively spliced transcript variants have been identified, but the full-length nature of only two transcript variants has been determined. Human HSD10 cDNA was cloned from brain (NM_004493), and the resulting protein, a homotetramer, was first characterized as a short chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD). Active sites of this enzyme can accommodate different substrates; 17β-HSD10 is involved in the oxidation of isoleucine, branched-chain fatty acids, and xenobiotics as well as the metabolism of sex hormones and neuroactive steroids.

17β-Hydroxysteroid dehydrogenase 2 (17β-HSD2) is an enzyme of the 17β-hydroxysteroid dehydrogenase (17β-HSD) family that in humans is encoded by the HSD17B2 gene.

Carbonyl reductase 1, also known as CBR1, is an enzyme which in humans is encoded by the CBR1 gene. The protein encoded by this gene belongs to the short-chain dehydrogenases/reductases (SDR) family, which function as NADPH-dependent oxidoreductases having wide specificity for carbonyl compounds, such as quinones, prostaglandins, and various xenobiotics. Alternatively spliced transcript variants have been found for this gene.

Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating is an enzyme that in humans is encoded by the NSDHL gene. This enzyme is localized in the endoplasmic reticulum and is involved in cholesterol biosynthesis.

3-keto-steroid reductase is an enzyme that in humans is encoded by the HSD17B7 gene.

Retinol dehydrogenase 11 is an enzyme that in humans is encoded by the RDH11 gene.

Estradiol 17 beta-dehydrogenase 8 is an enzyme that in humans is encoded by the HSD17B8 gene.

Dehydrogenase/reductase SDR family member 2 is an enzyme that in humans is encoded by the DHRS2 gene.

Retinol dehydrogenase 12 is an enzyme that in humans is encoded by the RDH12 gene.

Dehydrogenase/reductase SDR family member 1, also known as Short chain dehydrogenase/reductase family 19C member 1 is an enzyme that in humans is encoded by the DHRS1 gene located on chromosome 14.

Estradiol 17-beta-dehydrogenase 12 is an enzyme that in humans is encoded by the HSD17B12 gene.

Short-chain dehydrogenase/reductase 3 is an enzyme that in humans is encoded by the DHRS3 gene.

Dehydrogenase/reductase SDR family member 9 is an enzyme that in humans is encoded by the DHRS9 gene.

Hydroxysteroid 17-beta dehydrogenase 6 is an enzyme that in humans is encoded by the HSD17B6 gene.

Dehydrogenase/reductase SDR family member 4 is an enzyme that in humans is encoded by the DHRS4 gene.

Dehydrogenase/reductase member 7B is an enzyme encoded by the DHRS7B gene in humans, found on chromosome 17p11.2. DHRS7B encodes a protein that is predicted to function in steroid hormone regulation. A deletion in the chromosomal region 17p11.2 has been associated with Smith-Magenis Syndrome, a genetic developmental disorder.

Retinol dehydrogenase 13 (all-trans/9-cis) is a protein that in humans is encoded by the RDH13 gene. This gene encodes a mitochondrial short-chain dehydrogenase/reductase, which catalyzes the reduction and oxidation of retinoids. The encoded enzyme may function in retinoic acid production and may also protect the mitochondria against oxidative stress. Alternatively spliced transcript variants have been described.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000100612 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000021094 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Entrez Gene: Dehydrogenase/reductase (SDR family) member 7" . Retrieved 2014-04-28.
↑ Araya S, Kratschmar DV, Tsachaki M, Stücheli S, Beck KR, Odermatt A (July 2017). "DHRS7 (SDR34C1) – A new player in the regulation of androgen receptor function by inactivation of 5α-dihydrotestosterone?". The Journal of Steroid Biochemistry and Molecular Biology. 171: 288–295. doi:10.1016/j.jsbmb.2017.04.013. PMID 28457967.
↑ Štambergová H, Zemanová L, Lundová T, Malčeková B, Skarka A, Šaft M, Wsól V (January 2016). "Human DHRS7, promising enzyme in metabolism of steroids and retinoids?". Journal of Steroid Biochemistry and Molecular Biology. 155, Part A: 112–119. doi:10.1016/j.jsbmb.2015.09.041. PMID 26466768.

Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jörnvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U (March 2009). "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chemico-Biological Interactions. 178 (1–3): 94–8. doi:10.1016/j.cbi.2008.10.040. PMC 2896744 . PMID 19027726.
Ramasamy A, Curjuric I, Coin LJ, Kumar A, McArdle WL, Imboden M, Leynaert B, Kogevinas M, Schmid-Grendelmeier P, Pekkanen J, Wjst M, Bircher AJ, Sovio U, Rochat T, Hartikainen AL, Balding DJ, Jarvelin MR, Probst-Hensch N, Strachan DP, Jarvis DL (November 2011). "A genome-wide meta-analysis of genetic variants associated with allergic rhinitis and grass sensitization and their interaction with birth order". The Journal of Allergy and Clinical Immunology. 128 (5): 996–1005. doi: 10.1016/j.jaci.2011.08.030 . PMID 22036096.
Štambergová H, Škarydová L, Dunford JE, Wsól V (January 2014). "Biochemical properties of human dehydrogenase/reductase (SDR family) member 7". Chemico-Biological Interactions. 207: 52–7. doi:10.1016/j.cbi.2013.11.003. PMID 24246706.
Skarka A, Škarydová L, Štambergová H, Wsól V (March 2014). "Purification and reconstitution of human membrane-bound DHRS7 (SDR34C1) from Sf9 cells". Protein Expression and Purification. 95: 44–49. doi:10.1016/j.pep.2013.11.013. PMID 24316191.
Seibert JK, Quagliata L, Quintavalle C, Hammond TG, Terracciano L, Odermatt A (November 2015). "A role for the dehydrogenase DHRS7 (SDR34C1) in prostate cancer". Cancer Medicine. 4 (11): 1717–1729. doi:10.1002/cam4.517. PMC 4673999 . PMID 26311046.
Zemanová L, Kirubakaran P, Pato IH, Štambergová H, Vondrášek J (December 2017). "The identification of new substrates of human DHRS7 by molecular modeling and in vitro testing". International Journal of Biological Macromolecules. 105, Part 1: 171–182. doi:10.1016/j.ijbiomac.2017.07.012. PMID 28687384.
Stücheli S, Araya S, Ercan C, Moser SO, Gallon J, Jenö P, Piscuoglio S, Terracciano L, Odermatt A (June 2022). "The Potential Tumor-Suppressor DHRS7 Inversely Correlates with EGFR Expression in Prostate Cancer Cells and Tumor Samples". Cancers (Basel). 14 (13). doi:10.3390/cancers14133074. PMC 9264982 . PMID 35804847.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000100612 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000021094 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: Dehydrogenase/reductase (SDR family) member 7" . Retrieved 2014-04-28.

[6] Araya S, Kratschmar DV, Tsachaki M, Stücheli S, Beck KR, Odermatt A (July 2017). "DHRS7 (SDR34C1) – A new player in the regulation of androgen receptor function by inactivation of 5α-dihydrotestosterone?". The Journal of Steroid Biochemistry and Molecular Biology. 171: 288–295. doi:10.1016/j.jsbmb.2017.04.013. PMID 28457967.

[7] Štambergová H, Zemanová L, Lundová T, Malčeková B, Skarka A, Šaft M, Wsól V (January 2016). "Human DHRS7, promising enzyme in metabolism of steroids and retinoids?". Journal of Steroid Biochemistry and Molecular Biology. 155, Part A: 112–119. doi:10.1016/j.jsbmb.2015.09.041. PMID 26466768.

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DHRS7

Contents

Function

Related Research Articles

References

Further reading